Cynomolgus SerpinC1 / AntithrombinIII Protein (His Tag)

Serpin peptidase inhibitor, clade C (antithrombin), member 1 Protein Datasheet

SerpinC1 / SERPINC1 / AntithrombinIII Protein Product Information

• Synonym: SerpinC1
• Protein Construction: A DNA sequence encoding the Cynomolgus (Macaca fascicularis) SerpinC1 (Met 1- Ser 464) was fused with a polyhistidine tag at the C-terminus.
• Source: Cynomolgus
• Expression Host: Human Cells

SerpinC1 / SERPINC1 / AntithrombinIII Protein QC Testing

• Purity: > 95 % as determined by SDS-PAGE.
• Bio-activity: Measured by its ability to inhibit thrombin cleavage of a fluorogenic peptide substrate Boc-VPR-AMC, R&D Systems, Catalog# ES011.
  The IC₅₀ value is <5 nM.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Ser 35
• Molecular Mass: The recombinant cynomolgus SerpinC1 consists of 441 amino acids and has a calculated molecular mass of 50.2 kDa. The apparent molecular mass of the recombinant protein is approximately 55-60 KDa in SDS-PAGE under reducing conditions due to glycosylation.
• Formulation: Lyophilized from sterile PBS, pH7.4
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: SerpinC1 / SERPINC1 / AntithrombinIII protein

SerpinC1 / SERPINC1 / AntithrombinIII Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

SerpinC1 / SERPINC1 / AntithrombinIII Protein Description

SerpinC1, also known as antithrombin III (AT III), is a member of the serpin superfamily of serine protease inhibitors. SerpinC1 synthesized in the liver is the principal plasma serpin of blood coagulation proteases and inhibits thrombin and other factors such as Xa by the formation of covalently linked complexes. In common with SerpinA5 and D1, the inhibitory activity of SerpinC1 undergoes a dramatic increase in the presence of heparin and other glycosaminoglycans. The deficiency or functional abnormality of ATIII may result in an increased risk of thromboembolic disease, such as deep vein thrombosis and pulmonary embolism. In addition, it has been reported that SerpinC1 can alter or influence inflammatory processes via inhibition of NF-κB activation or actin polymerization.

References

1. Chandra, T. et al., 1983, Proc. Natl. Acad. Sci. 80: 1845-1848.
2. Perry, D.J. et al., 1994, Blood. Rev. 8: 37-55.
3. Chuang, Y.J. et al., 2001, Biochemistry. 40: 6670-6679.
4. Saito, H. et al., 2005, J. Leukoc. Biol. 78: 777-784.
5. Oelschlager, C. et al., 2002, Blood. 99: 4015-4020.